Antennapedia Peptide
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Antennapedia Peptide

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Antennapedia Peptide, a cell-penetrating 16 amino acid peptide originally derived from the 60 amino acid long homeodomain of the Drosophila transcription factor Antennapedia, is a member of the family of Cell-penetrating peptides.

Functional Peptides
Catalog number
CAS number
Molecular Formula
Molecular Weight
Antennapedia Peptide
(2S)-6-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-6-amino-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-amino-5-carbamimidamido-1-hydroxypentylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1-hydroxy-3-methylpentylidene]amino]-1-hydroxyhexylidene]amino]-1-hydroxy-3-methylpentylidene]amino]-1-hydroxy-3-(1H-indol-3-yl)propylidene]amino]-1-hydroxy-3-phenylpropylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1,4-dihydroxy-4-iminobutylidene]amino]-5-carbamimidamido-1-hydroxypentylidene]amino]-5-carbamimidamido-1-hydroxypentylidene]amino]-1-hydroxy-4-methylsulfanylbutylidene]amino]-1-hydroxyhexylidene]amino]-1-hydroxy-3-(1H-indol-3-yl)propylidene]amino]-1-hydroxyhexylidene]amino]hexanoic acid
L-Arginyl-L-glutaminyl-L-isoleucyl-L-lysyl-L-isoleucyl-L-tryptophyl-L-phenylalanyl-L-glutaminyl-L-asparaginyl-L-arginyl-L-arginyl-L-methionyl-L-lysyl-L-tryptophyl-L-lysyl-L-lysine; N5-(diaminomethylidene)-L-ornithyl-L-glutaminyl-L-isoleucyl-L-lysyl-L-isoleucyl-L-tryptophyl-L-phenylalanyl-L-glutaminyl-L-asparaginyl-N5-(diaminomethylidene)-L-ornithyl-N5-(diaminomethylidene)-L-ornithyl-L-methionyl-L-lysyl-L-tryptophyl-L-lysyl-L-lysine; Penetratin; Penetratin-1; Arg-Gln-Ile-Lys-Ile-Trp-Phe-Gln-Asn-Arg-Arg-Met-Lys-Trp-Lys-Lys
1.4±0.1 g/cm3
Store at -20°C
Soluble in Water, DMSO
InChI Key
Canonical SMILES
1. Selective inhibition of NLRP3 inflammasome by designed peptide originating from ASC
Žiga Strmšek,Iva Hafner-Bratkovič,Duško Lainšček,Petra Sušjan,Gregor Anderluh,Vesna Hodnik FASEB J . 2020 Aug;34(8):11068-11086. doi: 10.1096/fj.201902938RR.
NACHT, LRR, and PYD domains-containing protein 3 (NLRP3) inflammasome is a multiprotein complex which forms within cells in response to various microbial and self-derived triggers. Mutations in the gene encoding NLRP3 cause rare cryopyrin-associated periodic syndromes (CAPS) and growing evidence links NLRP3 inflammasome to common diseases such as Alzheimer's disease. In order to modulate different stages of NLRP3 inflammasome assembly nine peptides whose sequences correspond to segments of inflammasome components NLRP3 and apoptosis-associated speck-like protein containing a CARD (ASC) were selected. Five peptides inhibited IL-1β release, caspase-1 activation and ASC oligomerization in response to soluble and particulate NLRP3 triggers. Modulatory peptides also attenuated IL-1β maturation induced by constitutive CAPS-associated NLRP3 mutants. Peptide corresponding to H2-H3 segment of ASC pyrin domain selectively inhibited NLRP3 inflammasome by binding to NLRP3 pyrin domain in the micromolar range. The peptide had no effect on AIM2 and NLRC4 inflammasomes as well as NF-κB pathway. The peptide effectively dampened neutrophil infiltration in the silica-induced peritonitis and when equipped with Antennapedia or Angiopep-2 motifs crossed the blood-brain barrier in a mouse model. Our study demonstrates that peptides represent an important tool for targeting multiprotein inflammatory complexes and can serve as the basis for the development of novel anti-inflammatory strategies for neurodegeneration.
2. Characterisation of cell-penetrating peptide-mediated peptide delivery
Mark A Lindsay,Ken Bundell,Peter Newham,Richard Christison,Sarah M V Brockbank,Catherine J Voyce,Simon W Jones Br J Pharmacol . 2005 Aug;145(8):1093-102. doi: 10.1038/sj.bjp.0706279.
Cell-penetrating peptides such as antennapedia, TAT, transportan and polyarginine have been extensively employed for in vitro and in vivo delivery of biologically active peptides. However, little is known of the relative efficacy, toxicity and uptake mechanism of individual protein transduction domain-peptide conjugates, factors that will be critical in determining the most effective sequence. In the present study, we show by FACS analysis that unconjugated antennapedia, TAT, transportan and polyarginine demonstrate similar kinetic uptake profiles, being maximal at 1-3 h and independent of cell type (HeLa, A549 and CHO cell lines). A comparison of the magnitude of uptake of cell-penetrating peptide conjugates demonstrated that polyarginine=transportan>antennapedia>TAT. However, examination of cellular toxicity showed that antennapedia
3. Penetratin story: an overview
Edmond Dupont,Alain Joliot,Alain Prochiantz Methods Mol Biol . 2011;683:21-9. doi: 10.1007/978-1-60761-919-2_2.
Cell-penetrating peptides are short, often hydrophilic peptides that get access to the intracellular milieu. They have aroused great interest both in academic and applied research. First, cellular internalization of CPPs often involves the crossing of a biological membrane (plasma or vesicular), thus challenging the view of the nonpermeability of these structures to large hydrophilic molecules. Secondly, CPPs can drive the internalization of hydrophilic cargoes into cells, a rate-limiting step in the development of many therapeutic substances. Interestingly, the two mostly used CPPs, TAT and Penetratin peptides, are derived from natural proteins, HIV Tat and Antennapedia homeoprotein, respectively. The identification of the Penetratin peptide, summarized in this review, is intimately linked to the study of its parental natural protein.
4. Localized Delivery of Caveolin-1 Peptide Assisted by Ultrasound-Mediated Microbubble Destruction Potentiates the Inhibition of Nitric Oxide-Dependent Vasodilation Response
Amelia Ríos,Carlos A Franco-Urquijo,J Angel Navarro-Becerra,Bruno Escalante Ultrasound Med Biol . 2021 Jun;47(6):1559-1572. doi: 10.1016/j.ultrasmedbio.2021.02.003.
In the endothelium, nitric oxide synthase (eNOS) is the enzyme that generates nitric oxide, a key molecule involved in a variety of biological functions and cancer-related events. Therefore, selective inhibition of eNOS represents an attractive therapeutic approach for NO-related diseases and anticancer therapy. Ultrasound-mediated microbubble destruction (UMMD) conjugated with cell-permeable peptides has been investigated as a drug delivery system for effective delivery of anticancer molecules. We investigated the feasibility of loading antennapedia-caveolin-1 peptide (AP-Cav), a specific eNOS inhibitor, onto microbubbles to be delivered by UMMD in rat aortic endothelium. AP-Cav-loaded microbubbles (AP-Cav-MBs) and US parameters were characterized. Aortas were treated with UMMD for 30 s with 1.3 × 108MBs/mL AP-Cav (8 μM)-MBs at 100-Hz pulse repetition frequency, 0.5-MPa acoustic pressure, 0.5 mechanical index and 10% duty cycle. NO-dependent vascular responses were assessed using an isolated organ system, 21 h post-treatment. Maximal relaxation response was inhibited 61.8% ± 1.6% in aortas treated with UMMD-AP-Cav-MBs, while in aortas treated with previously disrupted AP-Cav-MBs and then US, the inhibition was 31.6% ± 1.6%. The vascular contractile response was not affected. The impact of UMMD was evaluated in aortas treated with free AP-Cav; 30 μM of free AP-Cav was necessary to reach an inhibition response similar to that obtained with UMMD-AP-Cav-MBs. In conclusion, UMMD enhances the delivery and potentiates the effect of AP-Cav in the endothelial layer of rat aorta segments.
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